3dkt

Crystal structure of Thermotoga maritima encapsulin

Method: X-RAY DIFFRACTION D_max: 228.2 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Maritimacin

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 120 PDB declaration: 120-meric（120） Consistent with protein copy count	Chain A； UniProt 1–265 Chain B； UniProt 1–265 Chain C； UniProt 1–265 Chain D； UniProt 1–265 Chain E； UniProt 1–265 Chain F； UniProt 1–265 Chain G； UniProt 1–265 Chain H； UniProt 1–265 Chain I； UniProt 1–265 Chain J； UniProt 1–265	Not recorded	Putative uncharacterized protein × 60 （Q9WZP3）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.1；292 K；0.1M citrate, 21.5% MPD (v/v), 0.25M ammonium acetate, pH5.1, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 3.10 Å R-free 0.239

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 3DKT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6WKV Cryo-EM structure of engineered variant of the Encapsulin from Thermotoga maritima (TmE) Deposited 2020-04-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain 0 1–265（265 aa） Chain 1 1–265（265 aa） Chain 2 1–265（265 aa） Chain 3 1–265（265 aa） Chain 4 1–265（265 aa） Chain 5 1–265（265 aa） Chain 6 1–265（265 aa） Chain 7 1–265（265 aa） Chain 8 1–265（265 aa） Chain 9 1–265（265 aa） Chain A 1–265（265 aa） Chain B 1–265（265 aa） Chain C 1–265（265 aa） Chain D 1–265（265 aa） Chain E 1–265（265 aa） Chain F 1–265（265 aa） Chain G 1–265（265 aa） Chain H 1–265（265 aa） Chain I 1–265（265 aa） Chain J 1–265（265 aa） Chain K 1–265（265 aa） Chain L 1–265（265 aa） Chain M 1–265（265 aa） Chain N 1–265（265 aa） Chain O 1–265（265 aa） Chain P 1–265（265 aa） Chain Q 1–265（265 aa） Chain R 1–265（265 aa） Chain S 1–265（265 aa） Chain T 1–265（265 aa） Chain U 1–265（265 aa） Chain V 1–265（265 aa） Chain W 1–265（265 aa） Chain X 1–265（265 aa） Chain Y 1–265（265 aa） Chain Z 1–265（265 aa） Chain a 1–265（265 aa） Chain b 1–265（265 aa） Chain c 1–265（265 aa） Chain d 1–265（265 aa） Chain e 1–265（265 aa） Chain f 1–265（265 aa） Chain g 1–265（265 aa） Chain h 1–265（265 aa） Chain i 1–265（265 aa） Chain j 1–265（265 aa） Chain k 1–265（265 aa） Chain l 1–265（265 aa） Chain m 1–265（265 aa） Chain n 1–265（265 aa） Chain o 1–265（265 aa） Chain p 1–265（265 aa） Chain q 1–265（265 aa） Chain r 1–265（265 aa） Chain s 1–265（265 aa） Chain t 1–265（265 aa） Chain u 1–265（265 aa） Chain v 1–265（265 aa） Chain w 1–265（265 aa） Chain x 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7K5W Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid Deposited 2020-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.	Resolution 2.00 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：K182D, E183D, Del(184-190)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 3.55 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：H187K	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：H187R	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.91 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：G186E,H187E,Y188E	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.84 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：Del(184-190)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane	Resolution 2.75 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：E184D,P189D, Del(185-188)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.96 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa）	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–265（265 aa）	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–265（265 aa）	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–265（265 aa）	Mutation：K182G, L190G, Del(182-189)	RBF RIBOFLAVIN × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds	Resolution 2.53 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–264（264 aa）	Not recorded	FMN FLAVIN MONONUCLEOTIDE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force	Resolution 3.30 Å
9Y8P Cryo-EM structure of Thermotoga maritima encapsulin shell Deposited 2025-09-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 1–265（265 aa） Chain AA 1–265（265 aa） Chain AB 1–265（265 aa） Chain B 1–265（265 aa） Chain BA 1–265（265 aa） Chain BB 1–265（265 aa） Chain C 1–265（265 aa） Chain CA 1–265（265 aa） Chain CB 1–265（265 aa） Chain D 1–265（265 aa） Chain DA 1–265（265 aa） Chain DB 1–265（265 aa） Chain E 1–265（265 aa） Chain EA 1–265（265 aa） Chain EB 1–265（265 aa） Chain F 1–265（265 aa） Chain FA 1–265（265 aa） Chain FB 1–265（265 aa） Chain G 1–265（265 aa） Chain GA 1–265（265 aa） Chain GB 1–265（265 aa） Chain H 1–265（265 aa） Chain HA 1–265（265 aa） Chain HB 1–265（265 aa） Chain I 1–265（265 aa） Chain IA 1–265（265 aa） Chain J 1–265（265 aa） Chain JA 1–265（265 aa） Chain K 1–265（265 aa） Chain KA 1–265（265 aa） Chain L 1–265（265 aa） Chain LA 1–265（265 aa） Chain M 1–265（265 aa） Chain MA 1–265（265 aa） Chain N 1–265（265 aa） Chain NA 1–265（265 aa） Chain O 1–265（265 aa） Chain OA 1–265（265 aa） Chain P 1–265（265 aa） Chain PA 1–265（265 aa） Chain Q 1–265（265 aa） Chain QA 1–265（265 aa） Chain R 1–265（265 aa） Chain RA 1–265（265 aa） Chain S 1–265（265 aa） Chain SA 1–265（265 aa） Chain T 1–265（265 aa） Chain TA 1–265（265 aa） Chain U 1–265（265 aa） Chain UA 1–265（265 aa） Chain V 1–265（265 aa） Chain VA 1–265（265 aa） Chain W 1–265（265 aa） Chain WA 1–265（265 aa） Chain X 1–265（265 aa） Chain XA 1–265（265 aa） Chain Y 1–265（265 aa） Chain YA 1–265（265 aa） Chain Z 1–265（265 aa） Chain ZA 1–265（265 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å

12 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MARIT_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–265； UniProt 1–265 Author chain B； PDBConstruct 1–265； UniProt 1–265 Author chain C； PDBConstruct 1–265； UniProt 1–265 Author chain D； PDBConstruct 1–265； UniProt 1–265 Author chain E； PDBConstruct 1–265； UniProt 1–265 Author chain F； PDBConstruct 1–265； UniProt 1–265 Author chain G； PDBConstruct 1–265； UniProt 1–265 Author chain H； PDBConstruct 1–265； UniProt 1–265 Author chain I； PDBConstruct 1–265； UniProt 1–265 Author chain J； PDBConstruct 1–265； UniProt 1–265

Putative uncharacterized protein

OrganismNot specified

UniProt Q9WZP3

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 120 PDB declaration: 120-meric（120） Consistent with protein copy count	Chain K； UniProt 106–113 Chain L； UniProt 106–113 Chain M； UniProt 106–113 Chain N； UniProt 106–113 Chain O； UniProt 106–113 Chain P； UniProt 106–113 Chain Q； UniProt 106–113 Chain R； UniProt 106–113 Chain S； UniProt 106–113 Chain T； UniProt 106–113	Fragment：;C-terminal encapsulin binding peptide, UNP residues 106-113' ;	Maritimacin × 60 （Q9WZP2）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.1；292 K；0.1M citrate, 21.5% MPD (v/v), 0.25M ammonium acetate, pH5.1, VAPOR DIFFUSION, SITTING DROP, temperature 292K	Resolution 3.10 Å R-free 0.239

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	Q9WZP3_THEMA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain K； PDBConstruct 1–8； UniProt 106–113 Author chain L； PDBConstruct 1–8； UniProt 106–113 Author chain M； PDBConstruct 1–8； UniProt 106–113 Author chain N； PDBConstruct 1–8； UniProt 106–113 Author chain O； PDBConstruct 1–8； UniProt 106–113 Author chain P； PDBConstruct 1–8； UniProt 106–113 Author chain Q； PDBConstruct 1–8； UniProt 106–113 Author chain R； PDBConstruct 1–8； UniProt 106–113 Author chain S； PDBConstruct 1–8； UniProt 106–113 Author chain T； PDBConstruct 1–8； UniProt 106–113

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3dkt
Deposition date deposition_date	2008-06-26
Structure title title	Crystal structure of Thermotoga maritima encapsulin
Keywords keywords	;enzyme encapsulation, nanocompartment, oxidative stress, ferritin-like protein, hk97-fold, Antibiotic, Antimicrobial, Bacteriocin, Cobalt, Hydrolase, Protease, Secreted, STRUCTURAL PROTEIN-VIRUS LIKE PARTICLE COMPLEX ;; STRUCTURAL PROTEIN/VIRUS LIKE PARTICLE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	64.23 Å
Radius of gyration Rg (electron density) rg_electron	64.51 Å
Forward intensity I(0) i0	1284330000.00
Molecular weight molecular_weight	311000.0 kDa
Excluded volume excluded_volume	393390 Å³
Envelope volume envelope_volume	669560 Å³
Hydration-shell volume shell_volume	89105 Å³
Envelope diameter envelope_diameter	225.3 Å
Shell Rg shell_rg	63.34 Å
Envelope Rg envelope_rg	61.48 Å
Shape Rg shape_rg	64.51 Å
Total Rg total_rg	64.47 Å
Total atoms total_atoms	21970
Residues n_residues	2720
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	228.2 Å
Rg (real space) rg_real	64.61 Å
Rg uncertainty (real space) rg_real_error	2.68 Å
I(0) (real space) i0_real	1.2840e+09
I(0) uncertainty (real space) i0_real_error	2.8130e+07
Rg (reciprocal space) rg_reciprocal	63.83 Å
I(0) (reciprocal space) i0_reciprocal	1282000000.0000
Solution quality estimate total_estimate	0.8597
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	66.6 Å
Skewness Skewness skewness	0.306
Kurtosis Kurtosis kurtosis	-0.747
Angular range angular_range	— – 0.1200 Å⁻¹
Current regularization parameter α current_alpha	0.0007
Highest regularization parameter α highest_alpha	45970000.0000
Real-space data points n_real_points	25
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.881

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Maritimacin
Molecular weight formula_weight	30516.8 kDa
EC 编号 ec_number	3.4.-.-
Source method src_method	nat
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	22070

MEFLKRSFAPLTEKQWQEIDNRAREIFKTQLYGRKFVDVEGPYGWEYAAHPLGEVEVLSDENEVVKWGLRKSLPLIELRATFTLDLWELDNLERGKPNVDLSSLEETVRKVAEFEDEVIFRGCEKSGVKGLLSFEERKIECGSTPKDLLEAIVRALSIFSKDGIEGPYTLVINTDRWINFLKEEAGHYPLEKRVEECLRGGKIITTPRIEDALVVSERGGDFKLILGQDLSIGYEDREKDAVRLFITETFTFQVVNPEALILLKF

Entity 2 Entity 2 polymer

Description description	Putative uncharacterized protein
Molecular weight formula_weight	816.9 kDa
Source method src_method	nat
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K,L,M,N,O,P,Q,R,S,T

GGDLGIRK

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	100

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7. Fold Classification (SCOP + CATH) 20 domains

CATH v4.4 (20 domains)

Domain ID domain_id	3dktA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktE01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktE02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktF01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktF02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktG01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktG02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktH01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktH02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktI01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktI02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

Domain ID domain_id	3dktJ01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2400 — Major capsid protein gp5 fold
Homologous superfamily homologous superfamily	30 —

Domain ID domain_id	3dktJ02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily	10 — hypothetical protein PF0899 domain

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8. Citations (1)

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Unit-cell length a length_a	669.040 Å
Unit-cell length b length_b	669.040 Å
Unit-cell length c length_c	669.040 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	960

Space group space_group	F 41 3 2
Space-group number int_tables_number	210
Crystal system crystal_system	—

Resolution resolution	3.104 Å
Low-resolution limit resolution_low	49.867 Å
R factor r_factor	0.2200
R_work r_work	0.2190
R_free r_free	0.2390

fit	/app/data/saxs_computation/dk/3dkt/3dkt.fit
pddf	/app/data/pr_computation/dk/3dkt/3dkt.pr.out
profile	/app/data/saxs_computation/dk/3dkt/3dkt.dat

Crystal structure of Thermotoga maritima encapsulin

1. Protein Identity and Related Structures Protein Identity & Related Structures

Maritimacin

State in the Current Structure

Other States of the Same Protein in the Database

Putative uncharacterized protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 20 domains

CATH v4.4 (20 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)